ExplorEnz: EC 3.4.21.50

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3.4.21.50

Accepted name:

lysyl endopeptidase

Reaction:

Preferential cleavage: Lys┼, including -Lys┼Pro-

Other name(s):

Achromobacter proteinase I (also see Comment); Achromobacter lyticus alkaline proteinase I; protease I; achromopeptidase; lysyl bond specific proteinase

Comments:

From Achromobacter lyticus [6]. Enzymes with similar specificity are produced by Lysobacter enzymogenes (Endoproteinase Lys-C; [3]) and Pseudomonas aeruginosa (Ps-1; [4]). In peptidase family S1 (trypsin family)

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 123175-82-6

References:

1.	Masaki, T., Tanabe, M., Nakamura, K. and Soejima, M. Studies on a new proteolytic enzyme from Achromobacter lyticus M497-1. I. Purification and some enzymatic properties. Biochim. Biophys. Acta 660 (1981) 44–50. [DOI] [PMID: 6791693]
2.	Masaki, T., Fujihasi, T., Nakamura, K. and Soejima, M. Studies on a new proteolytic enzyme from Achromobacter lyticus M497-1. II. Specificity and inhibition studies of Achromobacter protease I. Biochim. Biophys. Acta 660 (1981) 51–55. [DOI] [PMID: 6168293]
3.	Jekel, P.A., Weijer, W.J. and Beintema, J.J. Use of endoproteinase Lys-C from Lysobacter enzymogenes in protein sequence analysis. Anal. Biochem. 134 (1983) 347–354. [DOI] [PMID: 6359954]
4.	Elliott, B.W. and Cohen, C. Isolation and characterization of a lysine-specific protease from Pseudomonas aeruginosa. J. Biol. Chem. 261 (1986) 11259–11265. [PMID: 3090046]
5.	Ohara, T., Makino, K., Shinagawa, H., Nakata, A., Norioka, S. and Sakiyama, F. Cloning, nucleotide sequence, and expression of Achromobacter protease I gene. J. Biol. Chem. 264 (1989) 20625. [PMID: 2684982]
6.	Tsunasawa, S., Masaki, T., Hirose, M., Soejima, M. and Sakiyama, F. The primary structure and structural characteristics of Achromobacter lyticus protease I, a lysine-specific serine protease. J. Biol. Chem. 264 (1989) 3832–3839. [PMID: 2492988]

[EC 3.4.21.50 created 1983]